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Database: UniProt
Entry: A0A0D9NY22_METAN
LinkDB: A0A0D9NY22_METAN
Original site: A0A0D9NY22_METAN 
ID   A0A0D9NY22_METAN        Unreviewed;       438 AA.
AC   A0A0D9NY22;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=NEDD8-activating enzyme E1 catalytic subunit {ECO:0000256|ARBA:ARBA00015203, ECO:0000256|RuleBase:RU368009};
DE            EC=6.2.1.64 {ECO:0000256|ARBA:ARBA00023624, ECO:0000256|RuleBase:RU368009};
GN   ORFNames=H634G_05742 {ECO:0000313|EMBL:KJK78927.1};
OS   Metarhizium anisopliae BRIP 53293.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium.
OX   NCBI_TaxID=1291518 {ECO:0000313|EMBL:KJK78927.1, ECO:0000313|Proteomes:UP000054544};
RN   [1] {ECO:0000313|Proteomes:UP000054544}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BRIP 53293 {ECO:0000313|Proteomes:UP000054544};
RX   PubMed=25102932; DOI=10.1186/1471-2164-15-660;
RA   Pattemore J.A., Hane J.K., Williams A.H., Wilson B.A., Stodart B.J.,
RA   Ash G.J.;
RT   "The genome sequence of the biocontrol fungus Metarhizium anisopliae and
RT   comparative genomics of Metarhizium species.";
RL   BMC Genomics 15:660-660(2014).
CC   -!- FUNCTION: Catalytic subunit of the dimeric E1 enzyme, which activates
CC       NEDD8. {ECO:0000256|RuleBase:RU368009}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + [NEDD8 protein] + [E1 NEDD8-activating enzyme]-L-
CC         cysteine = AMP + diphosphate + [E1 NEDD8-activating enzyme]-S-[NEDD8
CC         protein]-yl-L-cysteine.; EC=6.2.1.64;
CC         Evidence={ECO:0000256|ARBA:ARBA00024626,
CC         ECO:0000256|RuleBase:RU368009};
CC   -!- PATHWAY: Protein modification; protein neddylation.
CC       {ECO:0000256|ARBA:ARBA00005032, ECO:0000256|RuleBase:RU368009}.
CC   -!- SIMILARITY: Belongs to the ubiquitin-activating E1 family. UBA3
CC       subfamily. {ECO:0000256|ARBA:ARBA00006310,
CC       ECO:0000256|RuleBase:RU368009}.
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DR   EMBL; KE384732; KJK78927.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0D9NY22; -.
DR   STRING; 1291518.A0A0D9NY22; -.
DR   UniPathway; UPA00885; -.
DR   Proteomes; UP000054544; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0019781; F:NEDD8 activating enzyme activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0045116; P:protein neddylation; IEA:UniProtKB-UniRule.
DR   CDD; cd01488; Uba3_RUB; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   Gene3D; 1.10.10.520; Ubiquitin activating enzymes (Uba3). Chain: B, domain 2; 1.
DR   Gene3D; 3.10.290.20; Ubiquitin-like 2 activating enzyme e1b. Chain: B, domain 3; 1.
DR   InterPro; IPR014929; E2-binding.
DR   InterPro; IPR045886; ThiF/MoeB/HesA.
DR   InterPro; IPR000594; ThiF_NAD_FAD-bd.
DR   InterPro; IPR023318; Ub_act_enz_dom_a_sf.
DR   InterPro; IPR030468; Uba3_N.
DR   InterPro; IPR035985; Ubiquitin-activating_enz.
DR   PANTHER; PTHR10953:SF6; NEDD8-ACTIVATING ENZYME E1 CATALYTIC SUBUNIT; 1.
DR   PANTHER; PTHR10953; UBIQUITIN-ACTIVATING ENZYME E1; 1.
DR   Pfam; PF08825; E2_bind; 1.
DR   Pfam; PF00899; ThiF; 1.
DR   SMART; SM01181; E2_bind; 1.
DR   SUPFAM; SSF69572; Activating enzymes of the ubiquitin-like proteins; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU368009};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU368009};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU368009};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054544};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW   ECO:0000256|RuleBase:RU368009}.
FT   DOMAIN          352..436
FT                   /note="E2 binding"
FT                   /evidence="ECO:0000259|SMART:SM01181"
SQ   SEQUENCE   438 AA;  49293 MW;  C1087A11B84171B7 CRC64;
     MSISTQSTPD YGTINEEARW KYIDHIRRTP GPFTDPEATS EEFLAQFEKI KVLVIGAGGL
     GCEILKNLAM SKFKDIHVID MDTIDVSNLN RQFLFRSSDV GKYKAEVAAR FVQNRVKGVT
     ITAHNNRIQD FDETFYKQFQ LVICGLDSIE ARRWINAMLV SIAEEYEADT DSIKPLIDGG
     TEGFKGQSRV ILPSMTSCIE CQLDMHAPRA AVPLCTIASI PRQPEHCIEW AHVIAWEEEK
     PFPSLDKDEP EHVTWIYQKA LARAQEFGIS GVTYSLTQGT IKNIIPAIAS TNAIIAASCC
     NEAFKIATNS APCLGFENNY MMYSGNDSIY TYTFKHEKKD DCPVCGRKAR PLEVDPKVTL
     RELVDSFATR PEAQLKKPSI RAEGRTLYMQ FPPGLEKQTR PNLDKTIMDL GLIDGQQVVV
     TDPAFPLEFN FFFKFKEA
//
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